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Yusuf Hamied Department of Chemistry

 

Royal Society University Research Fellow

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Research

Dr Pietro Sormanni is a group leader supported by a Royal Society University Research Fellowship. His research focuses on the development of innovative data-driven technologies of rational antibody design, to obtain antibodies against targets that have been challenging to access using conventional approaches, and to improve or predict biophysical properties crucial for the successful development of antibody therapeutics. In his work he has established numerous collaborations and industrial partnerships, whose outcomes are beginning to demonstrate that computational approaches can be applied alongside established procedures to streamline antibody development, and to offer time- and cost-effective novel alternatives.  

Antibodies are key tools to address questions in biomedical research, are widely employed in diagnostics, and are increasingly used as therapeutics to treat many diseases, including cancer and neurodegeneration. Existing methods of antibody discovery and optimisation rely on the laboratory screening of large numbers of variants produced by library construction or by the immune system, which can be time consuming and costly, and sometimes result in antibodies exhibiting sub-optimal properties. Conversely, computational design could drastically reduce time and costs of antibody discovery, and in principle allow for a highly controlled parallel screening of multiple biophysical properties. Moreover, rational design inherently allows targeting specific regions on the target protein (epitopes), which can be particularly daunting using available techniques but is very important for many therapeutic applications.

Background

Prior to taking up this post, Pietro held a postdoctoral Borysiewicz Biomedical Sciences  Fellowship from the University of Cambridge, obtained a PhD in Chemistry from the University of Cambridge, and an MSc in Theoretical Physics from the University of Milan.

Join our group

We are always looking for talented and enthusiastic individuals to join the team. If you are interested, please get in touch to discuss potential opportunities.

 

Watch Dr Sormanni give a seminar on the group's research (April 2025).

 

 

Dr Sormanni discusses his research

Tour of the Sormanni lab

Publications

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.
FA Aprile, P Sormanni, M Perni, P Arosio, S Linse, TPJ Knowles, CM Dobson, M Vendruscolo
– Science Advances
(2017)
3,
e1700488
Simultaneous quantification of protein order and disorder.
P Sormanni, D Piovesan, GT Heller, M Bonomi, P Kukic, C Camilloni, M Fuxreiter, Z Dosztanyi, RV Pappu, MM Babu, S Longhi, P Tompa, AK Dunker, VN Uversky, SCE Tosatto, M Vendruscolo
– Nat Chem Biol
(2017)
13,
339
Correction for Perni et al., A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
M Perni, C Galvagnion, A Maltsev, G Meisl, MBD Mueller, PK Challa, JB Kirkegaard, P Flagmeier, SIA Cohen, R Cascella, SW Chen, R Limboker, P Sormanni, GT Heller, FA Aprile, N Cremades, C Cecchi, F Chiti, EAA Nollen, TPJ Knowles, M Vendruscolo, A Bax, M Zasloff, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
e2543
A natural product inhibits the initiation of α-synuclein aggregation & suppresses its toxicity
M Perni, C Galvagnion, A Maltsev, G Meisl, MBD Müller, PK Challa, JB Kirkegaard, P Flagmeier, SIA Cohen, R Cascella, SW Chen, R Limboker, P Sormanni, GT Heller, FA Aprile, N Cremades, C Cecchi, F Chiti, EAA Nollen, TPJ Knowles, M Vendruscolo, A Bax, M Zasloff, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
E1009
A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.
R Freer, P Sormanni, G Vecchi, P Ciryam, CM Dobson, M Vendruscolo
– Science Advances
(2016)
2,
e1600947
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.
C Camilloni, BM Sala, P Sormanni, R Porcari, A Corazza, M De Rosa, S Zanini, A Barbiroli, G Esposito, M Bolognesi, V Bellotti, M Vendruscolo, S Ricagno
– Scientific Reports
(2016)
6,
25559
Targeting disordered proteins with small molecules using entropy.
GT Heller, P Sormanni, M Vendruscolo
– Trends Biochem Sci
(2015)
40,
491
A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate.
FA Aprile, P Sormanni, M Vendruscolo
– Biochemistry
(2015)
54,
5103
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins
P Sormanni, FA Aprile, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2015)
112,
9902
The s2D method: Simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins
P Sormanni, C Camilloni, P Fariselli, M Vendruscolo
– Journal of Molecular Biology
(2015)
427,
982
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Research Group

Research Interest Group

Email address

ps589@cam.ac.uk

College

Clare Hall